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Volumn 293, Issue , 2012, Pages 197-205

Elastic and viscoelastic properties of a type I collagen fiber

Author keywords

Collagen fiber; Incremental stress relaxation; Rat tail tendons; Structural model; Viscoelastic model

Indexed keywords

COLLAGEN TYPE 1;

EID: 80155155991     PISSN: 00225193     EISSN: 10958541     Source Type: Journal    
DOI: 10.1016/j.jtbi.2011.10.018     Document Type: Article
Times cited : (29)

References (24)
  • 1
    • 77956652151 scopus 로고    scopus 로고
    • Restraining cross-links responsible for the mechanical properties of collagen fibers: natural and artificial
    • Avery N., Bailey A. Restraining cross-links responsible for the mechanical properties of collagen fibers: natural and artificial. Collagen 2008, 81-110.
    • (2008) Collagen , pp. 81-110
    • Avery, N.1    Bailey, A.2
  • 2
    • 69749098113 scopus 로고    scopus 로고
    • Mechanical properties and collagen cross-linking of the patellar tendon in old and young men
    • Couppe C., Hansen P., Kongsgaard M., Kovanen V., Suetta C., Aagaard P. Mechanical properties and collagen cross-linking of the patellar tendon in old and young men. J. Appl. Physiol. 2009, 107:880-886.
    • (2009) J. Appl. Physiol. , vol.107 , pp. 880-886
    • Couppe, C.1    Hansen, P.2    Kongsgaard, M.3    Kovanen, V.4    Suetta, C.5    Aagaard, P.6
  • 3
    • 0020531821 scopus 로고
    • The organization of crosslinking in collagen fibrils
    • Davison P.F., Brennan M. The organization of crosslinking in collagen fibrils. Connect. Tissue Res. 1983, 11:135-151.
    • (1983) Connect. Tissue Res. , vol.11 , pp. 135-151
    • Davison, P.F.1    Brennan, M.2
  • 4
    • 33749011438 scopus 로고    scopus 로고
    • A micromechanics-based model for the Mullins effect
    • De Tommasi D., Puglisi G., Saccomandi G. A micromechanics-based model for the Mullins effect. J. Rheol. 2006, 50:495.
    • (2006) J. Rheol. , vol.50 , pp. 495
    • De Tommasi, D.1    Puglisi, G.2    Saccomandi, G.3
  • 5
    • 0024588491 scopus 로고
    • Separation methods for the study of collagen and treatment of collagen disorders
    • Deyl Z., Adam M. Separation methods for the study of collagen and treatment of collagen disorders. J. Chromatogr. 1989, 448:161-197.
    • (1989) J. Chromatogr. , vol.448 , pp. 161-197
    • Deyl, Z.1    Adam, M.2
  • 6
    • 33748854428 scopus 로고    scopus 로고
    • Collagen cross-links
    • Eyre D.R., Wu J.J. Collagen cross-links. Collagen 2005, 207-229.
    • (2005) Collagen , pp. 207-229
    • Eyre, D.R.1    Wu, J.J.2
  • 8
    • 70350383075 scopus 로고    scopus 로고
    • Probabilistic constitutive law for damage in ligaments
    • Guo Z., De Vita R. Probabilistic constitutive law for damage in ligaments. Med. Eng. Phys. 2009, 31:1104-1109.
    • (2009) Med. Eng. Phys. , vol.31 , pp. 1104-1109
    • Guo, Z.1    De Vita, R.2
  • 9
    • 74849088007 scopus 로고    scopus 로고
    • In situ multi-level analysis of viscoelastic deformation mechanisms in tendon collagen
    • Gupta H.S., Seto J., Krauss S., Boesecke P., Screen H.R.C. In situ multi-level analysis of viscoelastic deformation mechanisms in tendon collagen. J. Struct. Biol. 2010, 169:183-191.
    • (2010) J. Struct. Biol. , vol.169 , pp. 183-191
    • Gupta, H.S.1    Seto, J.2    Krauss, S.3    Boesecke, P.4    Screen, H.R.C.5
  • 11
  • 12
    • 0030875449 scopus 로고    scopus 로고
    • Self-assembly of collagen fibers. Influence of fibrillar alignment and decorin on mechanical properties
    • Pins G.D., Christiansen D.L., Patel R., Silver F.H. Self-assembly of collagen fibers. Influence of fibrillar alignment and decorin on mechanical properties. Biophys. J. 1997, 73:2164-2172.
    • (1997) Biophys. J. , vol.73 , pp. 2164-2172
    • Pins, G.D.1    Christiansen, D.L.2    Patel, R.3    Silver, F.H.4
  • 14
    • 33744827688 scopus 로고    scopus 로고
    • Failure process of a bundle of plastic fibers
    • Raischel F., Kun F., Herrmann H. Failure process of a bundle of plastic fibers. Phys. Rev. E 2006, 73(6):66101.
    • (2006) Phys. Rev. E , vol.73 , Issue.6 , pp. 66101
    • Raischel, F.1    Kun, F.2    Herrmann, H.3
  • 15
    • 0036241448 scopus 로고    scopus 로고
    • Structural aspects of the extracellular matrix of the tendon: an atomic force and scanning electron microscopy study
    • Raspanti M., Congiu T., Guizzardi S. Structural aspects of the extracellular matrix of the tendon: an atomic force and scanning electron microscopy study. Arch. Histol. Cytol. 2002, 65:37-43.
    • (2002) Arch. Histol. Cytol. , vol.65 , pp. 37-43
    • Raspanti, M.1    Congiu, T.2    Guizzardi, S.3
  • 16
    • 0020017123 scopus 로고
    • Analysis of the crosslinking components in collagen and elastin
    • Robins S.P. Analysis of the crosslinking components in collagen and elastin. Methods Biochem. Anal. 1982, 28:330-379.
    • (1982) Methods Biochem. Anal. , vol.28 , pp. 330-379
    • Robins, S.P.1
  • 17
    • 0031281802 scopus 로고    scopus 로고
    • Single-column high-performance liquid chromatographic-fluorescence detection of immature, mature, and senescent cross-links of collagen
    • Saito M., Marumo K., Fujii K., Ishioka N. Single-column high-performance liquid chromatographic-fluorescence detection of immature, mature, and senescent cross-links of collagen. Anal. Biochem. 1997, 253:26-32.
    • (1997) Anal. Biochem. , vol.253 , pp. 26-32
    • Saito, M.1    Marumo, K.2    Fujii, K.3    Ishioka, N.4
  • 18
    • 0033870607 scopus 로고    scopus 로고
    • Role of storage on changes in the mechanical properties of tendon and self-assembled collagen fibers
    • Silver F., Christiansen D., Snowhill P., Chen Y. Role of storage on changes in the mechanical properties of tendon and self-assembled collagen fibers. Connect. Tissue Res. 2000, 41:155-164.
    • (2000) Connect. Tissue Res. , vol.41 , pp. 155-164
    • Silver, F.1    Christiansen, D.2    Snowhill, P.3    Chen, Y.4
  • 19
    • 0035155477 scopus 로고    scopus 로고
    • Transition from viscous to elastic-based dependency of mechanical properties of self-assembled type I collagen fibers
    • Silver F., Christiansen D., Snowhill P., Chen Y. Transition from viscous to elastic-based dependency of mechanical properties of self-assembled type I collagen fibers. J. Appl. Polym. Sci. 2001, 79:134-142.
    • (2001) J. Appl. Polym. Sci. , vol.79 , pp. 134-142
    • Silver, F.1    Christiansen, D.2    Snowhill, P.3    Chen, Y.4
  • 20
    • 0036924318 scopus 로고    scopus 로고
    • Viscoelastic properties of self-assembled type I collagen fibers: molecular basis of elastic and viscous behaviors
    • Silver F., Ebrahimi A., Snowhill P. Viscoelastic properties of self-assembled type I collagen fibers: molecular basis of elastic and viscous behaviors. Connect. Tissue Res. 2002, 43:569-580.
    • (2002) Connect. Tissue Res. , vol.43 , pp. 569-580
    • Silver, F.1    Ebrahimi, A.2    Snowhill, P.3
  • 21
    • 0035182849 scopus 로고    scopus 로고
    • Viscoelastic properties of human skin and processed dermis
    • Silver F., Freeman J., DeVore D. Viscoelastic properties of human skin and processed dermis. Skin Res. Technol. 2001, 7:18-23.
    • (2001) Skin Res. Technol. , vol.7 , pp. 18-23
    • Silver, F.1    Freeman, J.2    DeVore, D.3
  • 22
    • 0141453852 scopus 로고    scopus 로고
    • Collagen self assembly and the development of tendon mechanical properties
    • Silver F.H., Freeman J.W., Seehra G.P. Collagen self assembly and the development of tendon mechanical properties. J. Biomech. 2003, 36:1529-1553.
    • (2003) J. Biomech. , vol.36 , pp. 1529-1553
    • Silver, F.H.1    Freeman, J.W.2    Seehra, G.P.3
  • 23
    • 0026464899 scopus 로고
    • Quantitative analysis of collagen and elastin cross-links using a single-column system
    • Sims T., Bailey A.J. Quantitative analysis of collagen and elastin cross-links using a single-column system. J. Chromatogr. Biomed. Appl. 1992, 582:49-55.
    • (1992) J. Chromatogr. Biomed. Appl. , vol.582 , pp. 49-55
    • Sims, T.1    Bailey, A.J.2
  • 24
    • 0347241157 scopus 로고    scopus 로고
    • Role of secondary structure on the stress relaxation processes on rat tail tendon (RTT) collagen fibre
    • Usha R., Subramanian V., Ramasami T. Role of secondary structure on the stress relaxation processes on rat tail tendon (RTT) collagen fibre. Macromol. Biosci. 2001, 1:100-107.
    • (2001) Macromol. Biosci. , vol.1 , pp. 100-107
    • Usha, R.1    Subramanian, V.2    Ramasami, T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.